CD45/PTPRC (C-6His) (recombinant mouse)

Protein Construction: Recombinant Mouse Receptor-type Tyrosine-protein Phosphatase C is produced by our Mammalian expression system and the target gene encoding Gln26­Lys566 is expressed with a 6His tag at the C-terminus. Sequence: Gln26­-Lys566. Fusion tag: C-6His Endotoxin: < 1.0 EU per µg as determined by the LAL method. Apparent Molecular Mass: 120-160 kDa. Protein function: Protein tyrosine phosphatase, receptor type C (CD45), also known as PTPRC is a member of the protein tyrosine phosphatase (PTP) family which is known for its function to serve as signaling molecules and to regulate a variety of cellular processes such as cell proliferation, differentiation, mitotic cycle and oncogenic transformation. It is a variably glycosylated 180-220 kDa transmembrane protein that is abundantly expressed on all nucleated cells of hematopoietic origin. CD45 has several isoforms, expressed according to cell type, developmental stage and antigenic exposure. CD45 has been best studied in T cells, where it determines T cell receptor signaling thresholds. CD45 is moved into or out of the immunological synapse (IS) membrane microdomain depending on the relative influence of interaction with the extracellular galectin lattice or the intracellular actin cytoskeleton. Galectin interaction can be fine-tuned by varying usage of the heavily O-glycosylated spliced regions and sialylation of N-linked carbohydrates. Within the IS, CD45 dephosphorylates and negatively regulates the src family kinase, LCK. In other leukocytes, CD45 influences differentiation and links immunoreceptor signaling with cytokine secretion and cell survival, partially overlapping in function with DEP-1/CD148. CD45 deletion causes in severe immunodeficiency, while point mutations may be associated with autoimmune disorders. Protein function: Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN. Dephosphorylates LYN, and thereby modulates LYN activity. [The UniProt Consortium]